guanidine and guanosine diphosphate

guanidine has been researched along with guanosine diphosphate in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	1 (50.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	1 (50.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Bekesi, E; Kung, HF; Manne, V	1
Arbildua, JJ; Brunet, JE; Díaz-Espinoza, R; Garcés, AP; Lagos, R; Monasterio, O; Montecinos, F	1

Other Studies

2 other study(ies) available for guanidine and guanosine diphosphate

Article	Year
Ha-ras proteins exhibit GTPase activity: point mutations that activate Ha-ras gene products result in decreased GTPase activity. Proceedings of the National Academy of Sciences of the United States of America, 1985, Volume: 82, Issue:2 Topics: Amino Acid Sequence; Bacterial Proteins; Dithiothreitol; Electrophoresis, Polyacrylamide Gel; Escherichia coli; GTP Phosphohydrolases; Guanidine; Guanidines; Guanosine Diphosphate; Harvey murine sarcoma virus; Magnesium; Mutation; Phosphoric Monoester Hydrolases; Sarcoma Viruses, Murine; Time Factors	1985
Domain folding and flexibility of Escherichia coli FtsZ determined by tryptophan site-directed mutagenesis. Protein science : a publication of the Protein Society, 2007, Volume: 16, Issue:8 Topics: Amino Acid Sequence; Escherichia coli; Escherichia coli Proteins; GTP Phosphohydrolases; Guanidine; Guanosine Diphosphate; Guanosine Triphosphate; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Point Mutation; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Structure-Activity Relationship; Tryptophan	2007

Article

Year

Ha-ras proteins exhibit GTPase activity: point mutations that activate Ha-ras gene products result in decreased GTPase activity.

Proceedings of the National Academy of Sciences of the United States of America, 1985, Volume: 82, Issue:2

Topics: Amino Acid Sequence; Bacterial Proteins; Dithiothreitol; Electrophoresis, Polyacrylamide Gel; Escherichia coli; GTP Phosphohydrolases; Guanidine; Guanidines; Guanosine Diphosphate; Harvey murine sarcoma virus; Magnesium; Mutation; Phosphoric Monoester Hydrolases; Sarcoma Viruses, Murine; Time Factors

1985

Domain folding and flexibility of Escherichia coli FtsZ determined by tryptophan site-directed mutagenesis.

Protein science : a publication of the Protein Society, 2007, Volume: 16, Issue:8

Topics: Amino Acid Sequence; Escherichia coli; Escherichia coli Proteins; GTP Phosphohydrolases; Guanidine; Guanosine Diphosphate; Guanosine Triphosphate; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Point Mutation; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Structure-Activity Relationship; Tryptophan

2007